Zinc in PDB 7f3p: Crystal Structure of A Nadp-Dependent Alcohol Dehydrogenase Mutant in Apo Form

All present enzymatic activity of Crystal Structure of A Nadp-Dependent Alcohol Dehydrogenase Mutant in Apo Form:
1.1.1.80;

The structure of Crystal Structure of A Nadp-Dependent Alcohol Dehydrogenase Mutant in Apo Form, PDB code: 7f3p was solved by X.Han, Y.Bi, H.L.Wei, J.Gao, Q.Li, G.Qu, Z.T.Sun, W.D.Liu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.77 / 2.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	79.848, 132.713, 135.23, 90, 90, 90
R / Rfree (%)	18.1 / 23.7

The binding sites of Zinc atom in the Crystal Structure of A Nadp-Dependent Alcohol Dehydrogenase Mutant in Apo Form (pdb code 7f3p). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of A Nadp-Dependent Alcohol Dehydrogenase Mutant in Apo Form, PDB code: 7f3p:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Crystal Structure of A Nadp-Dependent Alcohol Dehydrogenase Mutant in Apo Form


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of A Nadp-Dependent Alcohol Dehydrogenase Mutant in Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:332.3 occ:1.00 CE1 A:HIS59 2.2 62.9 1.0 SG A:CYS37 2.3 79.9 1.0 NE2 A:HIS59 2.3 72.4 1.0 OD2 A:ASP150 2.6 55.3 1.0 CB A:CYS37 3.3 62.0 1.0 OG A:SER39 3.3 74.3 1.0 ND1 A:HIS59 3.5 60.1 1.0 CD2 A:HIS59 3.6 63.7 1.0 CG A:ASP150 3.8 45.2 1.0 CZ2 A:TRP110 3.8 70.5 1.0 CB A:SER39 4.0 67.8 1.0 CH2 A:TRP110 4.0 63.4 1.0 CG A:HIS59 4.2 56.2 1.0 OE2 A:GLU60 4.2 48.0 1.0 OD1 A:ASP150 4.4 46.1 1.0 CA A:CYS37 4.7 56.9 1.0 CD A:GLU60 4.8 46.4 1.0 N A:SER39 4.8 66.4 1.0 CB A:ASP150 4.9 37.5 1.0 CE A:MET151 4.9 43.3 1.0

Zinc binding site 2 out of 4 in the Crystal Structure of A Nadp-Dependent Alcohol Dehydrogenase Mutant in Apo Form


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of A Nadp-Dependent Alcohol Dehydrogenase Mutant in Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn401 b:200.6 occ:1.00 OD2 B:ASP150 2.1 59.3 1.0 NE2 B:HIS59 2.3 62.7 1.0 SG B:CYS37 2.3 82.2 1.0 CE1 B:HIS59 2.8 66.8 1.0 CB B:CYS37 3.2 67.3 1.0 CG B:ASP150 3.3 45.9 1.0 CD2 B:HIS59 3.6 54.7 1.0 CB B:SER39 3.9 66.1 1.0 OD1 B:ASP150 3.9 49.3 1.0 OE2 B:GLU60 3.9 55.8 1.0 CE B:MET151 4.1 35.6 1.0 ND1 B:HIS59 4.1 59.4 1.0 CB B:ASP150 4.4 37.9 1.0 CG B:HIS59 4.5 51.0 1.0 CD B:GLU60 4.6 50.8 1.0 CA B:CYS37 4.7 61.8 1.0 N B:SER39 4.7 63.9 1.0 OG B:SER39 4.8 60.4 1.0 CA B:SER39 5.0 64.3 1.0

Zinc binding site 3 out of 4 in the Crystal Structure of A Nadp-Dependent Alcohol Dehydrogenase Mutant in Apo Form


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of A Nadp-Dependent Alcohol Dehydrogenase Mutant in Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn402 b:73.5 occ:1.00 OD2 C:ASP150 2.0 32.5 1.0 NE2 C:HIS59 2.1 41.1 1.0 SG C:CYS37 2.3 52.8 1.0 CE1 C:HIS59 3.1 45.5 1.0 CD2 C:HIS59 3.1 38.5 1.0 CG C:ASP150 3.2 34.6 1.0 CB C:CYS37 3.4 40.3 1.0 C4N C:NAP401 3.6 72.8 1.0 C3N C:NAP401 3.7 71.4 1.0 OG C:SER39 3.7 60.5 1.0 C7N C:NAP401 3.8 67.1 1.0 OD1 C:ASP150 3.8 32.7 1.0 CB C:SER39 3.9 53.3 1.0 O7N C:NAP401 3.9 63.5 1.0 C5N C:NAP401 4.0 74.6 1.0 OE2 C:GLU60 4.1 33.2 1.0 ND1 C:HIS59 4.2 46.2 1.0 CG C:HIS59 4.2 41.1 1.0 CE C:MET151 4.3 24.3 1.0 C2N C:NAP401 4.3 78.7 1.0 CB C:ASP150 4.4 29.7 1.0 CD C:GLU60 4.5 31.5 1.0 C6N C:NAP401 4.5 77.8 1.0 N7N C:NAP401 4.5 73.4 1.0 N1N C:NAP401 4.6 80.8 1.0 CA C:CYS37 4.8 38.3 1.0 N C:SER39 4.9 52.7 1.0 CG C:GLU60 4.9 31.2 1.0 OE1 C:GLU60 5.0 30.1 1.0

Zinc binding site 4 out of 4 in the Crystal Structure of A Nadp-Dependent Alcohol Dehydrogenase Mutant in Apo Form


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of A Nadp-Dependent Alcohol Dehydrogenase Mutant in Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn401 b:101.4 occ:1.00 OD2 D:ASP150 2.2 43.1 1.0 NE2 D:HIS59 2.3 44.8 1.0 SG D:CYS37 2.3 76.6 1.0 CE1 D:HIS59 3.0 54.3 1.0 CB D:CYS37 3.1 49.0 1.0 CG D:ASP150 3.4 41.8 1.0 CD2 D:HIS59 3.5 42.2 1.0 CE D:MET151 4.0 30.2 1.0 CH2 D:TRP110 4.0 57.2 1.0 OD1 D:ASP150 4.1 39.0 1.0 CB D:SER39 4.1 55.2 1.0 OE2 D:GLU60 4.1 33.1 1.0 ND1 D:HIS59 4.2 55.4 1.0 CZ2 D:TRP110 4.3 64.1 1.0 CD D:GLU60 4.5 33.8 1.0 CB D:ASP150 4.5 29.6 1.0 CG D:HIS59 4.5 40.8 1.0 O D:HOH536 4.5 38.3 1.0 CA D:CYS37 4.5 47.8 1.0 OG D:SER39 4.8 62.7 1.0 OE1 D:GLU60 4.9 32.6 1.0 N D:SER39 5.0 51.8 1.0 CG D:GLU60 5.0 31.5 1.0

G.Qu, Y.Bi, B.Liu, J.Li, X.Han, W.Liu, Y.Jiang, Z.Qin, Z.Sun. Unlocking the Stereoselectivity and Substrate Acceptance of Enzymes: Proline Induced Loop Engineering Test. Angew.Chem.Int.Ed.Engl. 2021.
ISSN: ESSN 1521-3773
DOI: 10.1002/ANIE.202110793